ReviewPrion
The complexity and implications of yeast prion domains.
Review in Prion. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed.
- Dan forms condensates in neuroblasts and regulates nuclear architecture and progenitor competence in vivo.Nature communications · 2024Article
- The Increased Amyloidogenicity of Spike RBD and pH-Dependent Binding to ACE2 May Contribute to the Transmissibility and Pathogenic Properties of SARS-CoV-2 Omicron as Suggested by In Silico Study.International journal of molecular sciences · 2022Article
- Identifying Endogenous Cellular Proteins Destabilizing the Propagation of Swi1 Prion upon Overproduction.Viruses · 2022Article
- Defining Key Residues of the Swi1 Prion Domain in Prion Formation and Maintenance.Molecular and cellular biology · 2021Article
- Sequence determinants of in cell condensate morphology, dynamics, and oligomerization as measured by number and brightness analysis.Cell communication and signaling : CCS · 2021Article
- Protein assembly systems in natural and synthetic biology.BMC biology · 2020Review
- Loss of Elongator- and KEOPS-Dependent tRNA Modifications Leads to Severe Growth Phenotypes and Protein Aggregation in Yeast.Biomolecules · 2020Article
- Natural and pathogenic protein sequence variation affecting prion-like domains within and across human proteomes.BMC genomics · 2020Article
- Identifying Anti-prion Chemical Compounds Using a Newly Established Yeast High-Throughput Screening System.Cell chemical biology · 2019Article
- Mutagenesis-Based Characterization and Improvement of a Novel Inclusion Body Tag.Frontiers in bioengineering and biotechnology · 2019Article
- A brief overview of the Swi1 prion-[SWI+].FEMS yeast research · 2018Review
- Prion Replication in the Mammalian Cytosol: Functional Regions within a Prion Domain Driving Induction, Propagation, and Inheritance.Molecular and cellular biology · 2018Article
- Article
- Effects of Mutations on the Aggregation Propensity of the Human Prion-Like Protein hnRNPA2B1.Molecular and cellular biology · 2017Article
- Amino acid composition predicts prion activity.PLoS computational biology · 2017Article
- Generating new prions by targeted mutation or segment duplication.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Distinct amino acid compositional requirements for formation and maintenance of the [PSI⁺] prion in yeast.Molecular and cellular biology · 2015Article
- Article
- Article
- Yeast prions and human prion-like proteins: sequence features and prediction methods.Cellular and molecular life sciences : CMLS · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
1 author.
Funding
Abstract
Prions are infectious proteins with altered conformations converted from otherwise normal host proteins. While there is only one known mammalian prion protein, PrP, a handful of prion proteins have been identified in the yeast Saccharomyces cerevisiae. Yeast prion proteins usually have a defined region called prion domain (PrD) essential for prion properties, which are typically rich in glutamine (Q) and asparagine (N). Despite sharing several common features, individual yeast PrDs are generally intricate and divergent in their compositional characteristics, which potentially implicates their prion phenotypes, such as prion-mediated transcriptional regulations.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.